A rapid and quantitative technique for assessing IgG monomeric purity, calibrated with the NISTmAb reference material.

ABSTRACT: The fraction of intact monomer in a sample (moles/moles), the monomeric purity, is measured as a quality control in therapeutic monoclonal antibodies but is often unknown in research samples and remains a major source of variation in quantitative antibody-based techniques such as immunoassay development. Here, we describe a novel multiplex technique for estimating the monomeric purity and antigen affinity of research grade antibody samples. Light scattering was used to simultaneously observe the mass of antibody binding to biosensor surfaces functionalised with antigen (revealing Fab binding kinetics) or protein A/G (PAG). Initial estimates of monomeric purity in 7 antibody samples including a therapeutic infliximab biosimilar were estimated by observing a mass deficit on the PAG surface c

SUBMITTER: Reader PP 

PROVIDER: S-EPMC6718376 | biostudies-literature | 2019 Sep

REPOSITORIES: biostudies-literature